Lecture 15 - Enzymes, Kinetics, Inhibition & Control Flashcards

1
Q

an enzyme modifies _____

A

the reaction barrier

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2
Q

what are 2 models of enzymes?

A
  1. lock and key

2. induced fit

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3
Q

what does a typical enzyme kinetics experiment measure?

A

-initial rate (v0) as a function of substrate concentration [S]

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4
Q

What does the kinetics curve of an enzyme reaction look like?

A

a saturation binding curve

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5
Q

why does an enzyme reaction curve look similar to a saturation binding curve?

A

-because “turnover” is preceded by substrate/enzyme binding

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6
Q

What is turnover controlled by?

A

catalytic efficiency

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7
Q

what is enzymatic activity revealed by?

A

the rate of the production of P (the velocity of the reaction)

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8
Q

Enzyme kinetics is a function of ________ and _______ efficiency

A
  • binding

- catalytic

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9
Q

what is Km?

A

measure of enzyme-substrate binding affinity

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10
Q

what is Vmax?

A

measure of catalytic efficiency

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11
Q

[E]total =

A

[E] + [ES]

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12
Q

V0 =

A

Vmax[S]/Km+[S]

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13
Q

what is the interpretation of the Michaelis-Menten equation?

A

when [S]&raquo_space; [E]T, S saturates all the binding sites.

Vmax is proportional to [E]Txthe catalytic efficiency

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14
Q

kcat =

A

Vmax/[E]total

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15
Q

Linewaver-Burk plots

A

?

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